Complementation of the Fo c subunit of escherichia coli with that of streptococcus mutans and properties of the hybrid FoF1 ATP Synthase

Journal of Bacteriology

Volumn 195, Issue 21, 2013, Pages 4873-4878

  Araki, Makoto ^a   Hoshi, Kazuya ^a   Fujiwara, Masasuke ^b   Sasaki, Yuka ^c   Yonezawa, Hideo ^d   Senpuku, Hidenobu ^d   Iwamoto Kihara, Atsuko ^c   Maeda, Masatomo ^a  

^a IWATE MEDICAL UNIVERSITY   (Japan)

^b OSAKA UNIVERSITY   (Japan)

^c NAGAHAMA INSTITUTE OF BIO SCIENCE AND TECHNOLOGY   (Japan)

^d NATIONAL INSTITUTE OF INFECTIOUS DISEASES   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; HYBRID PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; RESTRICTION ENDONUCLEASE; SUCCINIC ACID; GLUCOSE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; PROTEIN SUBUNIT;

ARTICLE; BACTERIAL CELL; BACTERIAL ENDOCARDITIS; BACTERIAL GROWTH; BETA CHAIN; BINDING SITE; CODON USAGE; DENTAL CARIES; DNA SEQUENCE; ESCHERICHIA COLI; GENETIC COMPLEMENTATION; IN VITRO STUDY; NONHUMAN; NUCLEOTIDE SEQUENCE; OPERON; OXIDATIVE PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; STREPTOCOCCUS MUTANS; AMINO ACID SEQUENCE; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; PHYSIOLOGY; PROTEIN SUBUNIT;

AMINO ACID SEQUENCE; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, BACTERIAL; GENETIC COMPLEMENTATION TEST; GLUCOSE; PROTEIN SUBUNITS; PROTON-TRANSLOCATING ATPASES; STREPTOCOCCUS MUTANS;

EID: 84886038502     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00542-13     Document Type: Article

References (29)

1. +-ATPase): results by combined biochemical and molecular biological approaches. Annu. Rev. Biochem. 58:111-136.
2. 64→Ala substituted subunit c of Escherichia coli ATP synthase in which the essential proline is switched between transmembrane helices. J. Biol. Chem. 276:27449-27454.
3. 1 to Fo. J. Biol. Chem. 269:7532-7537.
4. Maeda M. 2008. ATP synthases: bioinformatics based insights into how their electrochemically driven motor comprised of subunits a and c might serve as a drug target. J. Bioenerg. Biomembr. 40:117-121.
5. Boyer PD. 1999. Molecular motors: what makes ATP synthase spin?. Nature 402:247-248.
6. Loesche WJ. 1986. Role of Streptococcus mutans in human dental decay. Microbiol. Rev. 50:353-380.
7. Ajdic D, McShan WM, McLaughlin RE, Savic G, Chang J, Carson MB, Primeaux C, Tian R, Kenton S, Jia H, Lin S, Qian Y, Li S, Zhu H, Najar F, Lai H, White J, Roe BA, Ferretti JJ. 2002. Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen. Proc. Natl. Acad. Sci. U. S. A. 99:14434-14439.
8. Quivey R.G. Jr, Kuhnert WL, Hahn K. 2001. Genetics of acid adaptation in oral Streptococci. Crit. Rev. Oral Biol. Med. 12:301-314.
9. Nomura R, Nakano K, Nemoto H, Fujita K, Inagaki S, Takahashi T, Taniguchi K, Takeda M, Yoshioka H, Amano A, Ooshima T. 2006. Isolation and characterization of Streptococcus mutans in heart valve and dental plaque specimens from a patient with infective endocarditis. J. Med. Microbiol. 55:1135-1140.
10. Andries K, Verhasselt P, Guillemont J, Göhlmann HWH, Neefs J-M, Winkler H, Gestel JV, Timmerman P, Zhu M, Lee E, Williams P, de Chaffoy D, Huitric E, Hoffner S, Cambau E, Truffot-Pernot C, Lounis N, Jarlier V. 2005. A diarylquinoline drug active on the ATP synthase of Mycobacterium tuberculosis. Science 307:223-227.
11. Koul A. Dendouga N, Vergauwen K, Molenberghs B, Vranskx L, Willebrords R, Ristic Z, Lill H, Dorange I, Guillemont J, Bald D, Andries K. 2007. Diarylquinolines target subunit c of mycobacterial ATP synthase. Nat. Chem. Biol. 3:323-324.
12. Klionsky DJ, Brusilow WSA, Simoni RD. 1984. In vivo evidence for the role of the epsilon subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli. J. Bacteriol. 160:1055-1060.
13. +-ATPase. J. Biol. Chem. 266:16350-16355.
14. Sanger F, Coulson AR, Barrell BG, Smith AJH, Roe BA. 1980. Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. J. Mol. Biol. 143:161-178.
15. Sambrook J, Fritsch EF, Maniatis T. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
16. +-ATPase is important for activity. J. Biol. Chem. 265:21279-21284.
17. Futai M, Sternweiss PC, Heppel LA. 1974. Purification and properties of reconstitutively active and inactive adenosinetriphosphatase from Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 71:2725-2729.
18. 1 ) and its reconstitution into liposomes with neurotransmitter transporters. J. Biol. Chem. 266:22141-22146.
19. Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
20. Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the bacteriophage T4. Nature 227:680-685.
21. Towbin H, Staehelin T, Gordon J. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U. S. A. 76:4350-4354.
22. o ATP synthase: 1H distance measurements to nitroxide-derivatized aspartyl- 61. Biochemistry 33:665-674.
23. o ATP synthase and SecE of the SecYEG translocase. Biochemistry 42: 10537-10544.
24. Xie D-L, Lill H, Hauska G, Maeda M, Futai M, Nelson N. 1993. The atp2 operon of the green bacterium. Chlorobium limicola. Biochim. Biophys. Acta 1172:267-273.
25. Kuhnert W.L. Quivey RG, Jr., 2003. Genetic and biochemical characterization of the F-ATPase operon from Streptococcus sanguis 10904. J. Bacteriol. 185:1525-1533.
26. Trüper HG, De'Clari L. 1997. Necessary correction of specific epithets formed as substantives (nouns) "in apposition." Int. J. Syst. Bacteriol. 47:908-909.
27. 24 in helix-1. J. Biol. Chem. 269:5473-5479.
28. +)- translocating function retained. Proc. Natl. Acad. Sci. U. S. A. 87:4900- 4904.
29. o ATPase subunit c and cytoplasmic pH regulation. J. Bacteriol. 183:1524-1530.